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Related Concept Videos

Selectins01:25

Selectins

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Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
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Cell Adhesion Molecules - Types and Functions01:20

Cell Adhesion Molecules - Types and Functions

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Cell adhesion molecules (CAMs) are pivotal to multicellularity and the coordinated functioning of tissues and organ systems. They enable physical interactions between cells and provide mechanical strength to tissues. They also function as receptors for signal transmission across the plasma membrane. The CAMs are broadly classified into four families - integrins, cadherins, selectins, and immunoglobulin-like CAMs (IgCAMs).
CAM Families
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The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
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Transduction01:16

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Among the three main modes of HGT—transformation, conjugation, and transduction—transduction is unique in that it is mediated by bacteriophages, or bacterial viruses.Transduction occurs in two ways. Generalized transduction occurs during the lytic cycle of a bacteriophage infection. In this process, bacteriophages infect bacterial cells, replicate within them, and ultimately cause cell lysis, releasing newly assembled virions. Occasionally, random fragments of the bacterial genome...
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Protein Complexes with Interchangeable Parts01:57

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Related Experiment Video

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F-Type Lectins: Structure, Function, and Evolution.

Gerardo R Vasta1, Chiguang Feng2

  • 1Department of Microbiology and Immunology, University of Maryland School of Medicine, UMB, and Institute of Marine and Environmental Technology, Columbus Center, Baltimore, MD, USA. gvasta@som.umaryland.edu.

Methods in Molecular Biology (Clifton, N.J.)
|April 20, 2020
PubMed
Summary
This summary is machine-generated.

F-type lectins (FTLs) are a diverse protein family with unique fucose recognition domains (FTLDs). Their varied structures and specificities enable crucial roles in immunity, fertilization, and microbial interactions.

Keywords:
BindinCytolysinEel agglutininF-type lectin familyFucolectinFucose-bindingSelf/nonself recognitionStructural fold

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • F-type lectins (FTLs) possess a distinct fucose recognition domain (FTLD) with a novel jellyroll fold.
  • FTLs exhibit unique carbohydrate- and calcium-binding motifs, distinguishing them within lectin families.

Purpose of the Study:

  • To explore the structural diversity and functional implications of the F-type lectin domain (FTLD).
  • To investigate the evolutionary distribution and functional diversification of FTLs.

Main Methods:

  • Structural analysis of the F-type lectin domain (FTLD).
  • Comparative analysis of FTL sequences and their domain architectures.
  • Examination of the taxonomic distribution of FTLDs.

Main Results:

  • FTLs display a range of FTLD multiples and combinations with other domains, leading to varied structures.
  • Differences in carbohydrate specificity among FTLDs and multiple FTL isoforms contribute to diverse ligand recognition.
  • FTLs are involved in innate immunity, fertilization, microbial adhesion, and pathogenesis.

Conclusions:

  • FTLs exhibit extensive structural and functional diversification, impacting self/nonself recognition.
  • The discontinuous taxonomic distribution of FTLDs suggests evolutionary events like secondary loss and lateral gene transfer.